Short Description
The Rock Imager 1000® is a fully automated imaging system designed for protein crystallization screening. It is possible to capture superior quality images of protein drops while learning critical information about the crystals. Multiple images of each drop can be captured with user-adjustable settings including exposure, polarization, and condenser aperture. It is possible to specify regions of interest within a drop to zoom into. The Rock Imager® will automatically capture those areas in high resolution.
Contact Person
Georg Mlynek PhD, Elisabeth Laurent PhD
Research Services
Please contact the Core Facility via bmca@boku.ac.at
Methods & Expertise for Research Infrastructure
The Rock Imager 1000® has a storage capacity for 500 crystallization plates (e.g. SBS, Linbro, Nextal, Terasaki/HLA, Lipid Cubic Phase (LCP) plates), regulates temperature and features various imaging modes:
• Visible light imaging: The standard imaging technique for screening used by most crystallographers.
• Ultraviolet (UV) imaging: Protein crystallization drops are illuminated with UV light and the fluorescence generated from aromatic amino acids like tryptophan are detected to create an image. If no fluorescence is detected within a crystal, then it lacks enough aromatic amino acids to produce a signal and is likely not protein. The UV imaging option is built into Rock Imager 1000® with all several automated features, including automated imaging, extended focus imaging (EFI), and regions of interest (ROIs) that can help to see crystals better. The Rock Imager 1000® UV imaging solution uses 100% UV-optimized components: UV-grade optics, a UV-sensitive camera, and UV lighting. This optimization is critical for achieving the best image quality and fastest imaging speed possible.
• Multi-Fluorescence Imaging (MFI): This mode of imaging uses up to three different wavelengths, utilizing both UV and visible fluorescence imaging. With UV & visible fluorescence imaging, it is easy to find hidden protein crystals & discriminate them from salt, even protein with little-to-no tryptophan. Also, it is possible to differentiate between crystals of a protein-protein complex and crystals of a single protein.